Glucose-1-phosphate adenylyltransferase
| glucose-1-phosphate adenylyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 2.7.7.27 | ||||||||
| CAS number | 9027-71-8 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / EGO | ||||||||
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In enzymology, a glucose-1-phosphate adenylyltransferase (EC 2.7.7.27) is an enzyme that catalyzes the chemical reaction
- ATP + alpha-D-glucose 1-phosphate diphosphate + ADP-glucose
Thus, the two substrates of this enzyme are ATP and alpha-D-glucose 1-phosphate, whereas its two products are diphosphate and ADP-glucose.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is ATP:alpha-D-glucose-1-phosphate adenylyltransferase. Other names in common use include ADP glucose pyrophosphorylase, glucose 1-phosphate adenylyltransferase, adenosine diphosphate glucose pyrophosphorylase, adenosine diphosphoglucose pyrophosphorylase, ADP-glucose pyrophosphorylase, ADP-glucose synthase, ADP-glucose synthetase, ADPG pyrophosphorylase, ADP:alpha-D-glucose-1-phosphate adenylyltransferase and AGPase. This enzyme participates in starch and sucrose metabolism.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 1YP2, 1YP3, and 1YP4.
References
- Ghosh HP, Preiss J (1966). "Adenosine diphosphate glucose pyrophosphorylase. A regulatory enzyme in the biosynthesis of starch in spinach leaf chloroplasts". J. Biol. Chem. 241 (19): 4491–504. PMID 5922972.
- Shen L; Preiss J (1965). "Biosynthesis of bacterial glycogen. I. Purification and properties of the adenosine diphosphoglucose pyrophosphorylase of Arthrobacter species NRRL B1973". J. Biol. Chem. 240: 2334–2340.